Abstract
Lipopolysaccharide (LPS) is an essential glycolipid of the outer membrane (OM) of Gram-negative bacteria with a tripartite structure: lipid A, oligosaccharide core and O antigen. Seven essential LPS-transport proteins (LptABCDEFG) move LPS to the cell surface. Lpt proteins are linked by structural homology, featuring a β-jellyroll domain that mediates protein–protein interactions and LPS binding. Analysis of LptA–LPS interaction by fluorescence spectroscopy is used here to evaluate the contribution of each LPS moiety in protein−ligand interactions, comparing the wild-type (wt) protein to the I36D mutant. In addition to a crucial role of lipid A, an unexpected contribution emerges for the core region in recognition and binding of Lpt proteins.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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